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  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Plant Science 94 (1993), S. 127-137 
    ISSN: 0168-9452
    Keywords: Protein kinases ; Protein phosphorylation ; Rice
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 176 (1991), S. 622-626 
    ISSN: 0006-291X
    Keywords: [abr] DNP-SG; S-(2,4-dinitrophenyl)-glutathione ; [abr] LTC"4; leukotriene C"4 ; [abr] LTD"4; leukotriene D"4 ; [abr] LTE"4; leukotriene E"4 ; [abr] NPG; p-nitrophenyl glucuronide
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 176 (1991), S. 622-626 
    ISSN: 0006-291X
    Keywords: [abr] DNP-SG; S-(2,4-dinitrophenyl)-glutathione ; [abr] LTC"4; leukotriene C"4 ; [abr] LTD"4; leukotriene D"4 ; [abr] LTE"4; leukotriene E"4 ; [abr] NPG; p-nitrophenyl glucuronide
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 86 (1993), S. 935-942 
    ISSN: 1432-2242
    Keywords: Rice ; Embryo proteins ; Endosperm proteins ; Leaf proteins ; Protein database
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Proteins extracted from embryos, endosperms and leaves of rice were separated by two-dimensional electrophoresis and relative molecular weights and isoelectric points were determined. The separated proteins were electroblotted onto a polyvinylidene difluoride membrane and 85 electroblotted proteins were analyzed by a gas-phase protein sequencer. The N-terminal amino-acid sequences of 27 out of 85 proteins were determined in this manner. The N-terminal regions of the remaining proteins could not be sequenced and they were inferred to have a blocking group at the N-terminus. Among proteins, 11 could be sequenced after deblocking by in situ treatment with pyroglutamyl peptidase. The internal amino-acid sequences of 23 proteins were determined by sequence analysis of peptides obtained by Cleveland peptide mapping. The amino-acid sequences determined here were compared with those of known plant and animal proteins. The concanavalin A-peroxidase method was used to determine whether the 85 proteins were glycosylated and the diagonal electrophoresis method was used to determine whether they contained disulphide bonding. Finally, we constructed a data-file of rice proteins including information on relative molecular weight, isoelectric point, amino-acid sequence, sequence homology, glycosylation, and the presence of disulphide bonding.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 98 (1999), S. 1304-1310 
    ISSN: 1432-2242
    Keywords: Key words Cold stress ; Leaf proteins ; Protein phosphorylation ; Rice ; 2D-PAGE
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The response of plants to cold stress is not well understood at the biochemical level, although it has been studied extensively at the ecological level. To investigate whether protein phosphorylation may play an important role in cold stress, we exposed rice seedlings to low temperatures, prepared protein extracts from the leaves and incubated these in the presence of [γ-32P]ATP. The proteins were then separated by two-dimensional polyacrylamide gel electrophoresis. While several proteins were found to be phosphorylated upon cold stress one protein, pp35, which has an isoelectric point of 8.0, was more phosphorylated than the others. The pp35 protein was found to be phosphorylated when rice seedlings were incubated for 6 h at 5°C before the leaf protein extract was prepared and radioactive labeling was performed. The pp35 was, however, significantly more phosphorylated in cold-tolerant rice varieties. Antibodies were raised against purified pp35 in adult rabbits. Using this pp35 antibody, which can recognize the RuBisCO large-chain subunit (LSU), and from amino acid sequencing of pp35, we were able to identify and confirm the pp35 protein as the fragment of RuBisCO LSU (EC 4.1.1.39). Phosphorylation of the RuBisCO LSU may be important in cold tolerance.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1432-2242
    Keywords: Rice ; Semidwarf near-isogenic line ; Semi-dwarfism-related proteins ; Glutelin ; Pyroglutamic acid
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Two semidwarfism-related proteins, SRP-1 and SRP-2, were detected as major spots in a long-culm rice cultivar, Norin 29 and its semidwarf near-isogenic line, SC-TN1, respectively, by two-dimensional gel electrophoresis (2D-PAGE). The testcross showed that SRP-1 and SRP-2 are controlled by codominant alleles, Srp-1 and Srp-2, respectively, at a single locus Srp. This locus was considered to be closely linked with the semidwarfing gene locus sd-1. SRP-1 and SRP-2 were separated by 2D-PAGE, electroblotted onto a polyvinylidene difluoride membrane, and sequenced by a gas-phase protein sequencer. The N-terminal amino acid sequences, however, could not be determined due to the blockage of the N-terminals of these proteins. After removal of the N-terminal residue with pyroglutamyl peptidase given to the membrane, the amino acid sequence in the N-terminal region was determined. The N-terminal and internal amino acid sequences of SRP-1 and SRP-2 were highly homologous with those of the glutelin α-subunits of seed endosperm storage protein, which were deduced by the cDNA sequences. In the seed endosperms of Norin 29 and SC-TN1, a total of eight glutelin α-subunits was identified by 2D-PAGE. The amino acid sequences in the N-terminal and internal regions of these proteins were determined. This experiment confirmed that SRP-1 and SRP-2 are almost identical in structure with the glutelin α5a- and α5b-subunits, respectively, which were identified in several organs such as endosperms, embryos, and leaves, unlike the other glutelin α-subunits.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Springer
    Theoretical and applied genetics 101 (2000), S. 355-363 
    ISSN: 1432-2242
    Keywords: Key words Cold stress ; Ca2+-dependent protein kinase ; In-gel phosphorylation assay ; Rice
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Ca2+-dependent protein kinases (CDPKs) play an important role in plant signal transduction. Protein kinase(s) activities induced by 5°C cold stress in rice (Oryza sativa L.) seedlings were investigated in both leaf and stem tissues in an early (up to 45 min) and late (up to 12 h) response study. The leaf had 37-, 47- and 55-kDa protein kinase activities, and the stem had 37-, 47- and 55-kDa protein kinase activities. A 16-kDa protein showed constitutive kinase activity in the rice seedling leaf and stem. It was further identified that the 47-kDa protein kinase activity induced by cold in both the cytosolic and membrane fractions of the stem was strictly Ca2+-dependent. This CDPK activitiy increased in the presence of the Ca2+ ionophore A23187 in stem segments, whereas it was decreased by the Ca2+ channel blocker, LaCl3, and the Ca2+ chelator, EGTA. The general protein kinase inhibitor, staurosporine, completely inhibited this CDPK activity in vitro, and both W7, a calmodulin antagonist, and H7, a protein kinase C inhibitor, could only partially decrease this activity. The protein phosphatase inhibitor, okadaic acid, increased CDPK activity. This CDPK activity was also induced by salt, drought stress and the phytohormone abscicic acid. Among the 18 rice varieties tested, this cold-induced 47-kDa CDPK activity was stronger in the cold-tolerant varieties than in the sensitive ones.
    Type of Medium: Electronic Resource
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